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Background <p>Tyrosine sulfation is a widespread posttranslational modification in mammals and is known to influence protein function and signaling. However, its functional significance during porcine preimplantation development remains poorly understood.</p> Results <p>In this study, we demonstrate that TPST2-mediated tyrosine sulfation is critical for early porcine embryonic development. <i>TPST2</i> is transcriptionally activated during zygotic genome activation by its antisense long noncoding RNA, termed <i>aTPST2</i>, which recruits MED4, a core subunit of the Mediator complex, to activate <i>TPST2</i> transcription <i>in cis</i>. Mechanistically, TPST2 mediates sulfation at tyrosine 39 (Y39) of TTYH3, enhancing its protein stability. The stabilized TTYH3 interacts with RAP1B to activate MAPK signaling, thereby ensuring proper embryonic development.</p> Conclusions <p>Our findings elucidate a compelling molecular mechanism by which tyrosine sulfation orchestrates porcine preimplantation development. Together, these results provide new insights into the developmental functions of tyrosine sulfation.</p>

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TPST2-mediated tyrosine sulfation orchestrates porcine preimplantation development

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月22日

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  • Jiaze Gao,
  • Chengpeng Wang,
  • Hongshuang Xie,
  • Guang Yang,
  • Qingbo Yang,
  • Cheng Huang,
  • Shijie Li,
  • Zhonghua Liu,
  • Tianyao He,
  • Zhi Yin,
  • Jun-Xue Jin,
  • Jiaqiang Wang

摘要

Background

Tyrosine sulfation is a widespread posttranslational modification in mammals and is known to influence protein function and signaling. However, its functional significance during porcine preimplantation development remains poorly understood.

Results

In this study, we demonstrate that TPST2-mediated tyrosine sulfation is critical for early porcine embryonic development. TPST2 is transcriptionally activated during zygotic genome activation by its antisense long noncoding RNA, termed aTPST2, which recruits MED4, a core subunit of the Mediator complex, to activate TPST2 transcription in cis. Mechanistically, TPST2 mediates sulfation at tyrosine 39 (Y39) of TTYH3, enhancing its protein stability. The stabilized TTYH3 interacts with RAP1B to activate MAPK signaling, thereby ensuring proper embryonic development.

Conclusions

Our findings elucidate a compelling molecular mechanism by which tyrosine sulfation orchestrates porcine preimplantation development. Together, these results provide new insights into the developmental functions of tyrosine sulfation.